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Information on EC 1.1.1.100 - 3-oxoacyl-[acyl-carrier-protein] reductase and Organism(s) Mycobacterium tuberculosis and UniProt Accession O53665

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IUBMB Comments
Exhibits a marked preference for acyl-carrier-protein derivatives over CoA derivatives as substrates.
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This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: O53665
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The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
Synonyms
beta-ketoacyl reductase, fabg1, beta-ketoacyl-acp reductase, fabg4, 3-oxoacyl-acp reductase, fabg3, beta-ketoacyl-acyl carrier protein reductase, 3-ketoacyl-acp reductase, fabg2, oar1p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-oxoacyl-AcpM reductase
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beta-ketoacyl reductase
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3-ketoacyl acyl carrier protein reductase
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-
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3-ketoacyl-ACP(CoA) reductase
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3-ketoacyl-acyl carrier protein reductase
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3-oxoacyl-AcpM reductase
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3-oxoacyl-thioester reductase
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3-oxoacyl-[ACP]reductase
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beta-ketoacyl acyl carrier protein (ACP) reductase
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beta-ketoacyl reductase
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-
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beta-ketoacyl thioester reductase
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-
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beta-ketoacyl-ACP reductase
beta-ketoacyl-acyl carrier protein reductase
beta-ketoacyl-[acyl-carrier protein] (ACP) reductase
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-
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NADPH-specific 3-oxoacyl-[acylcarrier protein]reductase
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reductase, 3-oxoacyl-[acyl carrier protein]
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP+ = a 3-oxoacyl-[acyl-carrier protein] + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
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oxidation
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-
-
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(3R)-3-hydroxyacyl-[acyl-carrier protein]:NADP+ oxidoreductase
Exhibits a marked preference for acyl-carrier-protein derivatives over CoA derivatives as substrates.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-34-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-oxohexanoyl-CoA + NADH + H+
(3R)-3-hydroxyhexanoyl-CoA + NAD+
show the reaction diagram
-
-
-
?
3-oxoacyl-[acyl-carrier protein] + NADPH
3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
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-
-
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r
acetoacetyl-CoA + NADPH
3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
-
-
-
-
r
acetoacetyl-CoA + NADPH + H+
D-3-hydroxybutyryl-CoA + NADP+
show the reaction diagram
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-
-
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-oxoacyl-[acyl-carrier protein] + NADPH
3-hydroxyacyl-[acyl-carrier protein] + NADP+
show the reaction diagram
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-
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-hydroxybutyryl-CoA
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noncompetitive product inhibition pattern
NADP+
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noncompetitive product inhibition pattern
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.165
acetoacetyl-CoA
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pH 7.6, 30°C
0.026
NADPH
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pH 7.6, 30°C
additional information
additional information
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detailed kinetic and thermodynamic analysis, solvent and multiple kinetic isotope effects, kinetic mechanism
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7
acetoacetyl-CoA
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pH 7.0, 25°C
7
NADPH
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pH 7.6, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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product inhibition kinetics, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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increase in alpha-secondary deuterium kinetic isotope effect values measured at pH 10 as compared to those obtained at pH 7 points to isotope- and pH-sensitive steps occurring concomitantly
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 10
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pH profile, pH-dependence analysis, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 37
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temperature profile
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with hexanoyl-CoA, hanging drop vapor diffusion method, using
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S140A
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mutant shows no enzymatic activity. S140A mutant does not bind to NADPH
S140T
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mutant shows no enzymatic activity. Mutant S140T shows impaired NADPH binding
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein, modified purification protocol
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
FabG4 expressed from vector pPLM192 as mitochondrial protein in the Saccharomyces cerevisiae oar1DELTA mutant strain. FabG4 can restore respiratory growth of Saccharomyces cerevisiae oar1DELTA cells and renews lipoic acid production
expressed in Escherichia coli
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expression in Escherichia coli
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expression in Streptomyces cerevisiae cells lacking 3-oxoacyl-ACP reductase
FabG1 expressed from vector pPLM189 as mitochondrial protein in the Saccharomyces cerevisiae oar1DELTA mutant strain. FabG1 can restore respiratory growth of Saccharomyces cerevisiae oar1DELTA cells and renews lipoic acid production
selection of an Escherichia coli, BL21(DE3)NH host that stably expresses mutant forms of 3-ketoacyl-ACP(CoA) reductase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Poletto, S.S.; da Fonseca, I.O.; de Carvalho, L.P.; Basso, L.A.; Santos, D.S.
Selection of an Escherichia coli host that expresses mutant forms of Mycobacterium tuberculosis 2-trans enoyl-ACP(CoA) reductase and 3-ketoacyl-ACP(CoA) reductase enzymes
Protein Expr. Purif.
34
118-125
2004
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Silva, R.G.; de Carvalho, L.P.; Blanchard, J.S.; Santos, D.S.; Basso, L.A.
Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein (ACP) reductase: kinetic and chemical mechanisms
Biochemistry
45
13064-13073
2006
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Silva, R.G.; Rosado, L.A.; Santos, D.S.; Basso, L.A.
Mycobacterium tuberculosis beta-ketoacyl-ACP reductase: alpha-secondary kinetic isotope effects and kinetic and equilibrium mechanisms of substrate binding
Arch. Biochem. Biophys.
471
1-10
2008
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Gurvitz, A.
The essential mycobacterial genes, fabG1 and fabG4, encode 3-oxoacyl-thioester reductases that are functional in yeast mitochondrial fatty acid synthase type 2
Mol. Genet. Genomics
282
407-416
2009
Mycobacterium tuberculosis, Mycobacterium tuberculosis (O53665), Mycobacterium tuberculosis (P9WGT3), Mycobacterium tuberculosis H37Rv (P9WGT3), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Rosado, L.A.; Caceres, R.A.; de Azevedo, W.F.; Basso, L.A.; Santos, D.S.
Role of Serine140 in the mode of action of Mycobacterium tuberculosis beta-ketoacyl-ACP Reductase (MabA)
BMC Res. Notes
5
526
2012
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Dutta, D.; Bhattacharyya, S.; Roychowdhury, A.; Biswas, R.; Das, A.
Crystal structure of hexanoyl-CoA bound to beta-ketoacyl reductase FabG4 of Mycobacterium tuberculosis
Biochem. J.
450
127-139
2013
Mycobacterium tuberculosis (O53665), Mycobacterium tuberculosis, Mycobacterium tuberculosis CDC 1551 (O53665)
Manually annotated by BRENDA team